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2-deoxy-2-fluoro-D-glucose 6-phosphate + H2O
2-deoxy-2-fluoro-D-glucose + phosphate
-
18F-labeled model substrate
-
-
ir
2-deoxy-2-fluoro-D-glucose-6-phosphate + H2O
2-deoxy-2-fluoro-D-glucose + phosphate
-
-
-
-
?
2-deoxy-D-glucose + diphosphate
?
-
-
-
-
?
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
5'-AMP + H2O
?
-
2.6% of the activity with D-glucose 6-phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
-
1.2% of the activity with D-glucose 6-phosphate
-
-
?
carbamoyl phosphate
phosphate + NH3 + CO2
carbamoyl-phosphate + glucose
glucose 6-phosphate + NH3 + CO2
carbamoyl-phosphate + H2O
phosphate + NH3 + CO2
-
-
-
?
D-galactose + diphosphate
?
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-mannose + diphosphate
?
-
-
-
-
?
D-mannose 6-phosphate + H2O
D-mannose + phosphate
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
diphosphate + H2O
2 phosphate
glucose + ADP
glucose 6-phosphate + AMP
-
-
-
-
?
glucose + ATP
glucose 6-phosphate + ADP
-
-
-
-
?
glucose + CDP
glucose 6-phosphate + CMP
-
-
-
-
?
glucose + CTP
glucose 6-phosphate + CDP
-
-
-
-
?
glucose + dCTP
glucose 6-phosphate + dCDP
-
-
-
-
?
glucose + GDP
glucose 6-phosphate + GMP
-
-
-
-
?
glucose + GTP
glucose 6-phosphate + GDP
-
-
-
-
?
glucose + ITP
glucose 6-phosphate + IDP
-
-
-
-
?
glucose + phosphoenolpyruvate
glucose 6-phosphate + pyruvate
-
-
-
-
?
glucose + phosphoramide
glucose + aminophosphate
-
-
-
-
?
glycerol + diphosphate
?
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
p-nitrophenylphosphate + H2O
p-nitrophenol + phosphate
-
1.4% of the activity with D-glucose 6-phosphate
-
-
?
additional information
?
-
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
a better substrate in disrupted vesicles at pH 5.5 and pH 6.5
-
?
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
-
only in disrupted vesicles
-
?
carbamoyl phosphate
phosphate + NH3 + CO2
-
-
-
-
?
carbamoyl phosphate
phosphate + NH3 + CO2
-
-
-
-
?
carbamoyl-phosphate + glucose
glucose 6-phosphate + NH3 + CO2
-
-
-
?
carbamoyl-phosphate + glucose
glucose 6-phosphate + NH3 + CO2
-
-
-
-
?
carbamoyl-phosphate + glucose
glucose 6-phosphate + NH3 + CO2
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme catalytic subunit expression is regulated independently from the glucose-6-phosphate transporter expression by metabolites, overview
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme is the key enzyme of the gluconeogenesis pathway, and is positively regulated by a extracellular multipolypeptide complex called counting factor, CF, or the CF component coutin, respectively, while the glucokinase activity is inhibited by CF, regulation overview
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Frog
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Frog
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
enzyme system is required in hepatic D-glucose phosphorylation
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
key enzyme in D-glucose homeostasis
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme plays a important role of providing D-glucose during starvation
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
G6Pase facilitates microsomal D-glucose 6-phosphate uptake by D-glucose 6-phosphate transporter
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
ir
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
key enzyme in glucose metabolism
-
-
ir
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Marmota sp.
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme is required for the final steps of glycogenolysis and gluconeogenesis
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the brain functional glucose-6-phosphatase complex is capable of endogenous glucose production from glucose 6-phosphate, independent of blood glucose
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Pachnoda ephippiata
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Phryganea sp.
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
best substrate in disrupted and not disrupted vesicles at pH 5.5 and pH 6.5
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
enzyme is one of the rate-limiting enzymes of hepatic glucogenesis
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme catalyses the terminal reaction of gluconegenesis and glycogenolysis and plays a major role in the contol of blood glucose levels
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
the enzyme is required for the final steps of glycogenolysis and gluconeogenesis
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
salamander
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Sarcophaga barbata
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
dietary regulation of the enzyme in the liver glucose metabolism, overview
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
enzyme catalyses the final step in both glycogenolysis and glyconeogenesis
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Turtle
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Turtle
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
Vespa vulgaris
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
-
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
-
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
-
23% of the activity with D-glucose 6-phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
best substrate in disrupted and not disrupted vesicles at pH 5.5 and pH 6.5
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
additional information
?
-
-
the role of the enzyme in muscle is either to produce glucose from glucose 6-phosphate derived from glycogen or to provide the enzymatic basis for a substrate cycle betwen glucose and glucose 6-phosphate in muscle to improve the sensitivity of the mechanism that regulates the rate of glucose phosphorylation
-
-
?
additional information
?
-
-
activities for EC 3.1.3.9, EC 3.6.1.1, and pyrophosphate-glucose phosphotransferase are due to a single enzyme
-
-
?
additional information
?
-
-
cells of Dictyostelium discoideum form groups of about 20000 cells. The group size is regulated in part by a negative feedback pathway mediated by a secreted multipolypeptide complex called counting factor. It appears that part of the counting factor signal transduction pathway involves inhibiting the activity of glucose-6-phosphatase, decreasing intracellular glucose levels and affecting the levels of other metabolites, to regulate group size
-
-
?
additional information
?
-
-
the enzyme is involved in the mobilization of glucose from liver cells
-
-
?
additional information
?
-
enzyme deficiency causes glycogen storage disease type Ia, GSD-Ia, overview
-
-
?
additional information
?
-
-
enzyme deficiency causes glycogen storage disease type Ia, GSD-Ia, overview
-
-
?
additional information
?
-
glucose-6-phosphatase mutations affect protein stability and cause glycogen storgae disease type Ia, GSD-Ia, determined in Argentina, overview
-
-
?
additional information
?
-
-
glucose-6-phosphatase mutations affect protein stability and cause glycogen storgae disease type Ia, GSD-Ia, determined in Argentina, overview
-
-
?
additional information
?
-
-
reduced enzyme activity in woodchuck model of hepatitis virus-induced hepatocellular carcinoma, overview
-
-
?
additional information
?
-
-
the role of the enzyme in muscle is either to produce glucose from glucose 6-phosphate derived from glycogen or to provide the enzymatic basis for a substrate cycle betwen glucose and glucose 6-phosphate in muscle to improve the sensitivity of the mechanism that regulates the rate of glucose phosphorylation
-
-
?
additional information
?
-
-
the role of the enzyme in muscle is either to produce glucose from glucose 6-phosphate derived from glycogen or to provide the enzymatic basis for a substrate cycle betwen glucose and glucose 6-phosphate in muscle to improve the sensitivity of the mechanism that regulates the rate of glucose phosphorylation
-
-
?
additional information
?
-
-
the role of the enzyme in muscle is either to produce glucose from glucose 6-phosphate derived from glycogen or to provide the enzymatic basis for a substrate cycle betwen glucose and glucose 6-phosphate in muscle to improve the sensitivity of the mechanism that regulates the rate of glucose phosphorylation
-
-
?
additional information
?
-
-
the biosynthetic activity of the enzyme may act in concert with glycogen synthase during amino-acid-induced glycogenesis from glucose. Amino acids may play a role in increasing biosynthetic activity of the enzyme
-
-
?
additional information
?
-
-
the enzyme probably plays a key role in the down-regulation of the calcium signal required for glycogen mobilization
-
-
?
additional information
?
-
-
the role of the enzyme in muscle is either to produce glucose from glucose 6-phosphate derived from glycogen or to provide the enzymatic basis for a substrate cycle betwen glucose and glucose 6-phosphate in muscle to improve the sensitivity of the mechanism that regulates the rate of glucose phosphorylation
-
-
?
additional information
?
-
-
the enzyme is involved in sleep
-
-
?
additional information
?
-
-
the main regulatory function of the enzyme is to buffer the glucose 6-phosphate concentration. Hyperglycemia stimulates glucose-6-phosphatase gene transcription
-
-
?
additional information
?
-
-
the activity of glucose-6-phosphate synthesis can serve as an adjunct to glucokinase in hepatic glucose phosphorylation and may function in liver-mediated, adjustable maintanance of blood glucose homeostasis
-
-
?
additional information
?
-
-
final step in gluconeogenesis
-
-
?
additional information
?
-
-
terminal reaction of the pathway of glycogenolysis and gluconeogenesis. Activity of the enzyme is influenced by changes of the phospholipids on the microsomal membrane
-
-
?
additional information
?
-
-
the multicomponent hepatic glucose 6-phosphatase system catalyzes the terminal step of the hepatic glucose production and plays a role in the regulation of blood glucose
-
-
?
additional information
?
-
-
endoplasmic stress may play a role in diabetes, and it results in increased enzyme activity in the liver, overview
-
-
?
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1-propyl-3-(pyridin-2-yl)thiourea
-
40.71% inhibition
1-[(4'-O-(E)-p-coumaroyl)-beta-D-glucopyranosyl]-oxy-2-phenol
-
-
1-[(6'-O-(E)-p-coumaroyl)-beta-D-glucopyranosyl]-oxy-2-phenol
-
-
1-[O-beta-D-glucopyranosyl(1->2)-beta-D-glucopyranosyl]-oxy-2-phenol
-
-
2-nitro-5-thiocyano-benzoic acid
-
-
2-oxoglutarate
-
in complex with Mg2+, inhibition at low substrate concentrations, inhibition of the translocase component of the glucose 6-phosphatase system
2-{[bis(hydrazine)methylene]amino}-4-methylpentanoic acid
-
2.61% inhibition
2-{[bis(hydrazino)methylene]amino}-3-(4-hydroxyphenyl)propanoic acid
-
6.61% inhibition
2-{[bis(hydrazino)methylene]amino}-3-hydroxybutanoic acid
-
11.68% inhibition
2-{[bis(hydrazino)methylene]amino}-3-hydroxypropanoic acid
-
10.56% inhibition
2-{[bis(hydrazino)methylene]amino}-3-methylpentanoic acid
-
3.37% inhibition
3,4-dicaffeoylquinic acid
-
-
3,4-dichlorobenzaldehyde dibenzylhydrazone
-
-
3-Mercaptopicolinic acid
-
inhibitor of D-glucose 6-phosphate translocase
3-methoxybenzaldehyde dibenzylhydrazone
-
-
4,4'-di-isothiocyanostilbene-2,2'-disulphonate
-
inhibitor of D-glucose 6-phosphate translocase
4,5-dicaffeoylquinic acid
-
-
4-(beta-D-glucopyranosyloxy) benzoic acid
-
-
4-caffeoylquinic acid
-
-
4-chlorobenzaldehyde dibenzylhydrazone
-
-
4-hydroxybenzaldehyde dibenzylhydrazone
-
-
4-maleimidylstilbene-2,2'-disulfonic acid
-
-
4-methoxybenzaldehyde dibenzylhydrazone
-
-
4-methoxyphenyl-[4-(4-methoxyphenyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridin-5-yl]methanone
4-methoxyphenyl-[4-(4-trifluoromethoxyphenyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridin-5-yl]methanone
5-((((iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid
-
-
5-caffeoylquinic acid
-
-
5-chlorotetrahydrothiophene-2-carbaldehyde dibenzylhydrazone
-
-
5-ethyltetrahydrofuran-2-carbaldehyde dibenzylhydrazone
-
-
alpha-phosphatidylinositol 3-monophosphate
-
-
alpha-phosphatidylinositol 4,5-diphosphate
-
-
alpha-phosphatidylinositol 4-monophosphate
-
-
apigenin-7-O-beta-D-glucopyranoside
-
-
apigenin-7-O-beta-D-glucuronic acid-6''-methyl ester
-
-
benzaldehyde dibenzylhydrazone
-
-
CoA
-
inhibits enzyme activity in intact microsomes
EGTA
-
inhibits enzyme activity in histone 2A-treated or alamethicin-treated microsomes, but has little effect on enzyme activity in intact microsomes
epicatechin gallate
-
acts similarly but less efficiently than epigallocatechin gallate
epigallocatechin gallate
-
increases latency of G6Pase, inhibitory effect is greater in intact than in permeabilized microsomes. It does not hinder microsomal D-glucose 6-phosphate uptake. Reduces activity of G6Pase through the inhibition of glucose efflux from the endoplasmic reticulum lumen; inhibition of enzyme in intact, but not in permeabilized microsome. Epigallocatechin gallate does not hinder microsomal glucose uptake, but inhibits microsomal glucose efflux thus inhibiting the enzyme through an elevated luminal glucose level
fatty-acyl-CoA
-
with chain-length equal to or higher than 16, at 0.001-0.002 mM, the inhibitory effect on the enzyme of untreated microsomes is either partially or totally cancelled, or even changes into an activation effect at higher concentrations, the inhibition is fully reversible in presence of bovine serum albumin. With medium chain-length, 10-14 carbons inhibit the enzyme of untreated microsomes in a dose-dependent manner in the range 0.001-0.02 mM, the higher the chain length, the stronger the inhibitory effect
gallocatechin gallate
-
increases latency of G6Pase, inhibitory effect is greater in intact than in permeabilized microsomes
Insulin
-
insulin causes a decrease in the activity of enzyme in the liver in vivo
-
isonicotinaldehyde dibenzylhydrazone
-
-
L-alpha-phosphatidylinositol 3,4,5-trisphosphate
-
-
L-alpha-phosphatidylinositol 3,4-diphosphate
-
-
myristoyl-CoA
-
uncompetitive inhibition of enzyme in untreated microsomes, non-competitive inhibition of enzyme from detergent-treated microsomes
N-(pyridine-2-yl)morpholine-4-carbothioamide
-
35.32% inhibition
N-(pyridine-2-yl)piperidine-4-carbothioamide
-
38.88% inhibition
nicotinaldehyde dibenzylhydrazone
-
-
oxaloacetate
-
in complex with Mg2+, inhibition at low substrate concentrations, inhibition of the translocase component of the glucose 6-phosphatase system
p-hydroxy mercury-phenylsulfonate
-
-
p-hydroxy mercurybenzoic acid
-
-
palmitoyl-CoA
-
inhibits enzyme activity in intact microsomes
Phenobarbital
-
the inhibition in dependence on the age of rats is studied
phosphoinositides
-
in order of decreasing efficiency: phosphatidylinositol, L-alpha-phosphatidylinositol 3,4,5-trisphosphate, L-alpha-phosphatidylinositol 3,4-diphosphate, alpha-phosphatidylinositol 4,5-diphosphate, alpha-phosphatidylinositol 3-monophosphate, alpha-phosphatidylinositol 4-monophosphate, phosphatidylinositol. Mechanism of inhibition with alpha-phosphatidylinositol 3,4-diphosphate, alpha-phosphatidylinositol 4,5-diphosphate or L-alpha-phosphatidylinositol 3,4,5-trisphosphate is competitive
-
pyridine-2-carbaldehyde dibenzylhydrazone
-
-
pyrocatechol-O-beta-D-glucopyranoside
-
-
quercetin-3-O-beta-D-glucopyranoside
-
-
S5627
-
potent linear competitive inhibitor of the translocase component of the multicomponent hepatic glucose 6-phosphatase system
-
silibinin
-
induces a dose-dependent inhibition of gluconeogenesis associated with a potent decrease in enzyme activity; inhibits gluconeogenesis and D-glucose 6-phosphate hydrolysis from either lactate/pyruvate, glycerol or fructose in a dose-dependent manner. Effect is stronger in intact than in permeabilized microsomes
sodium barbital
-
3 mM, complete inhibition
sodium pentobarbital
-
3 mM, complete inhibition
Svetol
-
commercial unroasted and decaffeinated green Coffea canephora extract, competive inhibition
-
tetrahydrofuran-2-carbaldehyde dibenzylhydrazone
-
-
tetrahydrothiophene-2-carbaldehyde dibenzylhydrazone
-
-
tosyl-L-Lys-chloromethyl ketone
-
inactivation of the enzyme in intact microsomes, no effect on enzyme in deoxycholate-modified microsomes
tosyl-L-Phe-chloromethyl ketone
-
inactivation of the enzyme in intact microsomes, no effect on enzyme in deoxycholate-modified microsomes
tosyl-lysyl-chloromethane
-
inhibitor of D-glucose 6-phosphate translocase
tosylphenylalanylchloromethane
-
inhibitor of D-glucose 6-phosphate translocase
vanadyl acetylacetonate
-
mixed-type inhibition
vanadyl sulfate
-
37% inhibition at 0.048 microM, competitive inhibition
-
4-methoxyphenyl-[4-(4-methoxyphenyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridin-5-yl]methanone
-
-
4-methoxyphenyl-[4-(4-methoxyphenyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridin-5-yl]methanone
-
-
4-methoxyphenyl-[4-(4-trifluoromethoxyphenyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridin-5-yl]methanone
-
-
4-methoxyphenyl-[4-(4-trifluoromethoxyphenyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridin-5-yl]methanone
-
-
chlorogenic acid
-
inhibitor of D-glucose 6-phosphate translocase
D-glucose
-
non-competitive inhibitor, irrespective of the presence of detergents
D-glucose
-
reduces the G6Pase activity both in intact and permeabilized liver microsomes in a concentration-dependent manner. Extent of inhibition is comparable with that achieved by epigallocatechin gallate in intact microsomes
molybdate
-
-
phosphate
-
-
phosphate
-
non-competitive inhibition in intact microsomes, but competitive in the presence of detergents
S3483
-
reversible inhibitor of the translocase component of the multicomponent hepatic glucose 6-phosphatase system
S3483
-
only depresses G6Pase activity in intact microsomes, thus increases latency
vanadate
-
-
vanadate
-
reduces activity both in intact and permeabilized microsomes and decreases latency
additional information
-
activity of glucose-6-phosphatase in crude microsomes from cells with high, normal, or low counting factor activity has a negative correlation with the amount of counting factor present in these cell lines. Molecules greater than 10 kDa from wild-type cells strongly repress activity of glucose-6-phosphatase in wild-type microsomes
-
additional information
-
The enzyme is inhibited by several amphiphilic compounds, such as fatty acids and acyl-CoAs, but the physioligal significance is questionable, since the liver contains a fatty-acyl CoA binding protein, which may well prevent this effect. Some thiol reagents inhibit enzyme activity much more in intact than in disrupted microsomes.
-
additional information
-
tumor necrosis factor inhibits the transcriptional rate of glucose-6-phosphatase in vivo and in vitro
-
additional information
-
insulin and epidermal growth factor inhibit basal mouse G6Pase fusion gene transcription
-
additional information
-
the effect of the short-chain aldehydes on the kinetic parameters increases with chain-length
-
additional information
-
a Pro metabolite inhibits glucose 6-phosphate hydrolysis and thus directs glucose 6-phosphate away from glucose production and towards glycogen
-
additional information
-
expression of dominant-negative versions of both cAMP response element-binding protein and CAAT/enhancer-binding protein blocks the glucose response of the proximal region in a dose-dependent manner
-
additional information
-
propyl gallate has no effect
-
additional information
-
a series of N,N-dibenzyl-N-benzylidnenhydrazine represent a novel class of potent competivitve D-glucose-6-phosphatase catalytic inhibitors using disrupted microsomes
-
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Nordlie, R.C.; Sukalski, K.A.
Multifunctional glucose 6-phosphatase: a critical review
The Enzymes of Biological Membranes, 2nd Ed. (Martonosi, A. V. , ed. ), Plenum, New York
2
349-398
1985
Bos taurus, Cyprinus carpio, Cavia porcellus, Gallus gallus, Cricetulus griseus, Oryctolagus cuniculus, Dictyostelium discoideum, Felis catus, Frog, Homo sapiens, Vicugna pacos, Lampetra ayresii, Platyrrhini, Mus musculus, Oncorhynchus mykiss, Rattus norvegicus, salamander
-
brenda
Countaway, J.L.; Waddel, I.D.; Burchell, A.; Arion, W.J.
The phosphohydrolase component of the hepatic microsomal glucose-6-phosphatase system is a 36.5-kilodalton polypeptide
J. Biol. Chem.
263
2673-2678
1988
Rattus norvegicus
brenda
Suzuki, S.; Toyota, T.; Suzuki, H.; Goto, Y.
Partial purification from human mononuclear cells and placental plasma membranes of an insulin mediator which stimulates pyruvate dehydrogenase and suppresses glucose-6-phosphatase
Arch. Biochem. Biophys.
235
418-426
1984
Homo sapiens
brenda
Sawaki, K.; Taguchi, R.; Ikezawa, H.
Studies on the interactions between phospholipids and membrane-bound enzymes in microsomes. Effects of phospholipases C on kinetic properties of the glucose-6-phosphatase system in rat liver microsomes
J. Biochem.
93
537-546
1983
Rattus norvegicus
brenda
Karnovsky, M.L.; Anchors, J.M.; Zoccoli, M.A.
Glucose-6-phosphatase from cerebrum
Methods Enzymol.
90
396-402
1982
Rattus norvegicus
brenda
Rymsa, B.; de Groot, H.
Partial purification of rat liver microsomal glucose-6-phosphatase on hydroxylapatite
Biol. Chem. Hoppe-Seyler
369
115-121
1988
Rattus norvegicus
brenda
Nordlie, R.C.
Kinetic examination of enzyme mechanisms involving branched reaction pathways--a detailed consideration of multifunctional glucose-6-phosphatase
Methods Enzymol.
87
319-353
1982
Mammalia
brenda
Burchell, A.; Burchell, B.
Identification and purification of a liver microsomal glucose 6-phosphatase
Biochem. J.
205
567-573
1982
Oryctolagus cuniculus
brenda
Jorgensen, B.M.; Agerbo, P.; Jensen, B.; Borresen, T.; Holmer, G.
Inhibition of microsomal glucose 6-phosphatase by unsaturated aliphatic aldehydes and ketones
Chem. Biol. Interact.
81
209-218
1992
Rattus norvegicus
brenda
Reczek, P.R.; Villee, C.A.
A purification of microsomal glucose-6-phosphatase from human tissue
Biochem. Biophys. Res. Commun.
107
1158-1165
1982
Homo sapiens
brenda
Surholt, B.; Newsholme, E.A.
Maximum activities and properties of glucose 6-phosphatase in muscles from vertebrates and invertebrates
Biochem. J.
198
621-629
1981
Acherontia atropos, Agrotis exclamationis, Alitta virens, Apis mellifera, Arctia caja, Bombus hortorum, Bombus pascuorum, Bombus terrestris, Bombus vestalis, Bombyx mori, Calliphora vicina, Cavia porcellus, Columba livia, Crangon crangon, Deilephila elpenor, Gallus gallus, Laothoe populi, Locusta migratoria, Manduca sexta, Mus musculus, Musca domestica, Noctua pronuba, Nymphalis urticae, Oryctolagus cuniculus, Pachnoda ephippiata, Passer domesticus, Phalera bucephala, Phryganea sp., Pieris brassicae, Protophormia terraenovae, Rana temporaria, Rattus norvegicus, Sarcophaga barbata, Schistocerca gregaria, Spilarctia lutea, Vespa vulgaris, Xenopus laevis
brenda
Bickerstaff, G.F.; Burchell, B.
Studies on the purification of glucose 6-phosphatase from rabbit liver microsomal fraction
Biochem. Soc. Trans.
8
389-390
1980
Oryctolagus cuniculus
brenda
Nordlie, R.C.; Jorgenson, R.A.
Glucose-6-phosphatase
The Enzymes of Biological Membranes (Martonosi, A. V. , ed. ) Plenum, New York
2
465-491
1976
Anas platyrhynchos, Bos taurus, Canis lupus familiaris, Gallus gallus, Columba livia, Cottus gobio, Oryctolagus cuniculus, Cervidae, Felis catus, Chondrichthyes, Ovis aries, Homo sapiens, Trochilidae, Mus musculus, Necturus maculosus, Lithobates catesbeianus, Rana sp., Rattus norvegicus, Thamnophis sirtalis, Turtle
-
brenda
Stetten, M.R.; Goldsmith, P.K.
A Limulus glucose-6-phosphatase with phosphotransferase activity characteristic of vertebrate liver microsomes. Its possible evolutionary significance
Biochim. Biophys. Acta
444
835-852
1976
Limulus sp.
brenda
Anchors, J.M.; Karnovsky, M.L.
Purification of cerebral glucose-6-phosphatase. An enzyme involved in sleep
J. Biol. Chem.
250
6408-6416
1975
Rattus norvegicus
brenda
Pederson, B.A.; Nordlie, M.A.; Foster, J.D.; Nordlie, R.C.
Effects of ionic strength and chloride ion on activities of the glucose-6-phosphatase system: regulation of the biosynthetic activity of glucose-6-phosphatase by chloride ion inhibition/deinhibition
Arch. Biochem. Biophys.
353
141-151
1998
Rattus norvegicus
brenda
Metzger, S.; Begleibter, N.; Barash, V.; Drize, O.; Peretz, T.; Shiloni, E.; Chajek-Shaul, T.
Tumor necrosis factor inhibits the transcriptional rate of glucose-6-phosphatase in vivo and in vitro
Metabolism
46
579-583
1997
Mus musculus
brenda
Nordlie, R.C.
Multifunctional hepatic glucose-6-phosphatase and the tuning' of blood glucose levels
Trends Biochem. Sci.
1
199-202
1976
Rattus norvegicus
-
brenda
Nordlie, R.C.
Metabolic regulation by multifunctional glucose-6-phosphatase
Curr. Top. Cell. Regul.
8
33-117
1974
Anas platyrhynchos, Canis lupus familiaris, Cavia porcellus, Gallus gallus, Columba livia, Oryctolagus cuniculus, Cervidae, Felis catus, Chondrichthyes, Ovis aries, Homo sapiens, Trochilidae, Mus musculus, Necturus maculosus, Lithobates catesbeianus, Rana sp., Rattus norvegicus, Thamnophis sirtalis, Turtle
brenda
Colilla, W.; Jorgenson, R.A.; Nordlie, R.C.
Mammalian carbamyl phosphate: glucose phosphotransferase and glucose-6-phosphate phosphohydrolase: extended tissue distribution
Biochim. Biophys. Acta
377
117-125
1975
Bos taurus, Rattus norvegicus
brenda
Gold, E.W.; Veitch, F.P.
Studies on a pyrophosphatase and glucose-6-phosphatase from Aspergillus oryzae
Biochim. Biophys. Acta
327
166-175
1973
Aspergillus oryzae
brenda
Cori, C.F.; Garland, R.C.; Wang Chang, H.F.
Purification of particulate glucose-6-phosphatase
Biochemistry
12
3126-3130
1973
Rattus norvegicus
brenda
Nordlie, R.C.
Glucose-6-phosphatase, hydrolytic and synthetic activities
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
543-610
1971
Anas platyrhynchos, Bos taurus, Canis lupus familiaris, Cavia porcellus, Gallus gallus, Columba livia, Astacoidea, Oryctolagus cuniculus, Equus caballus, Felis catus, Frog, Ovis aries, Homo sapiens, Lampetra sp., Marmota sp., Mesocricetus auratus, Platyrrhini, Mus musculus, Necturus maculosus, Rattus norvegicus, Sus scrofa
-
brenda
Benedetti, A.; Fulceri, M.; Ferro, M.; Comporti, M.
On a possible role for glucose-6-phosphatase in the regulation of liver cell cytosolic concentration
Trends Biochem. Sci.
11
284-285
1986
Rattus norvegicus
-
brenda
Mithieux, G.; Daniele, N.; Payrastre, B.; Zitoun, C.
Liver microsomal glucose-6-phosphatase is competitively inhibited by the lipid products of phosphatidylinositol 3-kinase
J. Biol. Chem.
273
17-19
1998
Rattus norvegicus
brenda
Speth, M.; Schulze, H.U.
The purification of a detergent-soluble glucose-6-phosphatase from rat liver
Eur. J. Biochem.
208
643-650
1992
Rattus norvegicus
brenda
Methieux, G.; Zitoun, C.
Mechanisms by which fatty-acyl-CoA esters inhibit or activate glucose-6-phosphasaes in intact and detergent-treated rat liver microsomes
Eur. J. Biochem.
235
799-803
1996
Rattus norvegicus
brenda
Claeyssens, S.; Chedeville, A.; Lavoinne, A.
Inhibition of protein phosphatases activates glucose-6-phosphatase in isolated rat hepatocytes
FEBS Lett.
315
7-10
1993
Rattus norvegicus
brenda
Bode, A.M.; Foster, J.D.; Nordlie, R.C.
Glyconeogenesis from L-proline involves metabolite inhibition of the glucose-6-phosphatase system
J. Biol. Chem.
267
2860-2863
1992
Rattus norvegicus
brenda
Fulceri, R.; Gamerucci, A.; Scott, H.M.; Giunti, R.; Burchell, A.; Benedetti, A.
Fatty acyl-CoA esters inhibit glucose-6-phosphatase in rat liver microsomes
Biochem. J.
307
391-397
1995
Rattus norvegicus
-
brenda
Aiston, S.; Trinh, K.Y.; Lange, A.J.; Newgard, C.B.; Agius, L.
Glucose-6-phosphatase overexpression lowers glucose 6-phosphate and inhibits glycogen synthesis and glycolysis in hepatocytes without affecting glucokinase translocation
J. Biol. Chem.
274
24559-24566
1999
Rattus norvegicus
brenda
Arion, W.J.; Canfield, W.K.; Callaway, E.S.; Burger, H.J.; Hemmerle, H.; Schubert, G.; Herling, A.W.; Oekonomopulos, R.
Direct evidence for the involvement of two glucose 6-phosphate-binding sites in the glucose-6-phosphatase activity of intact liver microsomes
J. Biol. Chem.
273
6223-6227
1998
Rattus norvegicus
brenda
Mithieux, G.; Vega, F.V.; Riou, J.P.
The liver glucose-6-phosphatase of intact microsomes is inhibited and displays sigmoid kinetics in the presence of alpha-ketoglutarate-magnesium and oxaloacetate-magnesium chelates
J. Biol. Chem.
265
20364-20368
1990
Rattus norvegicus
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Mus musculus
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Sequence variation between the mouse and human glucose-6-phosphatase catalytic subunit gene promoters results in differential activation by peroxisome proliferator activated receptor gamma coactivator-1alpha
Diabetologia
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Mus musculus (P35576), Mus musculus
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Homo sapiens (P35575)
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Homo sapiens
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Homo sapiens (P35575), Homo sapiens
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Homo sapiens, Mus musculus
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A polymorphism within the G6PC2 gene is associated with fasting plasma glucose levels
Science
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Homo sapiens
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Effect of treatment with cadmium on kinetic properties of Na(+), K(+)-ATPase and glucose-6-phosphatase activity in rat liver microsomes a correlative study on influence of lipid/phospholipid make-up
Toxicology
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Rattus norvegicus
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Phenolic glycosides from Dodecadenia grandiflora and their glucose-6-phosphatase inhibitory activity
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Rattus norvegicus
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Henry-Vitrac, C.; Ibarra, A.; Roller, M.; Merillon, J.M.; Vitrac, X.
Contribution of chlorogenic acids to the inhibition of human hepatic glucose-6-phosphatase activity in vitro by Svetol, a standardized decaffeinated green coffee extract
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Homo sapiens
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Evidence for transcriptional regulation of the glucose-6-phosphate transporter by HIF-1alpha: Targeting G6PT with mumbaistatin analogs in hypoxic mesenchymal stromal cells
Stem Cells
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2009
Mus musculus
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Joshi, A.K.; Rajini, P.S.
Reversible hyperglycemia in rats following acute exposure to acephate, an organophosphorus insecticide: role of gluconeogenesis
Toxicology
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Rattus norvegicus
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Barfell, A.; Crumbly, A.; Romani, A.
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2011
Rattus norvegicus
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Hayee, B.; Antonopoulos, A.; Murphy, E.J.; Rahman, F.Z.; Sewell, G.; Smith, B.N.; McCartney, S.; Furman, M.; Hall, G.; Bloom, S.L.; Haslam, S.M.; Morris, H.R.; Boztug, K.; Klein, C.; Winchester, B.; Pick, E.; Linch, D.C.; Gale, R.E.; Smith, A.M.; Dell, A.; Segal, A.W.
G6PC3 mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction
Glycobiology
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2011
Homo sapiens
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Mahato, A.; Bhattacharya, S.; Shanthi, N.
Design, synthesis and glucose-6-phosphatase inhibitory activity of diaminoguanidine analogues of 3-guanidinopropionic acid and amino substituted (pyridin-2-yl)thiourea derivatives
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Capra hircus
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Konopelska, S.; Kienitz, T.; Quinkler, M.
Downregulation of Hepatic Glucose-6-Phosphatase-alpha in Patients With Hepatic Steatosis
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Homo sapiens
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Shehzad, S.
The potential effect of vanadium compounds on glucose-6-phosphatase
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Bos taurus
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Moraes-Silva, L.; Bueno, T.M.; Franciscato, C.; de Oliveira, C.S.; Peixoto, N.C.; Pereira, M.E.
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Rattus norvegicus
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Homo sapiens
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Jeon, J.Y.; Lee, H.; Park, J.; Lee, M.; Park, S.W.; Kim, J.S.; Lee, M.; Cho, B.; Kim, K.; Choi, A.M.; Kim, C.K.; Yun, M.
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Homo sapiens
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Yoshida, M.; Lee, E.Y.; Kohno, T.; Tanaka, T.; Miyazaki, M.; Miki, T.
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Mueller, M.S.; Fouyssac, M.; Taylor, C.W.
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Soty, M.; Chilloux, J.; Delalande, F.; Zitoun, C.; Bertile, F.; Mithieux, G.; Gautier-Stein, A.
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Homo sapiens (P35575)
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Singh, P.; Han, E.H.; Endrizzi, J.A.; OBrien, R.M.; Chi, Y.I.
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Homo sapiens
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Mus musculus
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